1rla

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:23, 14 February 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rla.gif|left|200px]]
 
-
{{Structure
+
==THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE==
-
|PDB= 1rla |SIZE=350|CAPTION= <scene name='initialview01'>1rla</scene>, resolution 2.1&Aring;
+
<StructureSection load='1rla' size='340' side='right'caption='[[1rla]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
+
<table><tr><td colspan='2'>[[1rla]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RLA FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-
}}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rla OCA], [https://pdbe.org/1rla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rla RCSB], [https://www.ebi.ac.uk/pdbsum/1rla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rla ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rl/1rla_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rla ConSurf].
 +
<div style="clear:both"></div>
-
'''THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE'''
+
==See Also==
-
 
+
*[[Arginase 3D structures|Arginase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Each individual excretes roughly 10 kg of urea per year, as a result of the hydrolysis of arginine in the final cytosolic step of the urea cycle. This reaction allows the disposal of nitrogenous waste from protein catabolism, and is catalysed by the liver arginase enzyme. In other tissues that lack a complete urea cycle, arginase regulates cellular arginine and ornithine concentrations for biosynthetic reactions, including nitric oxide synthesis: in the macrophage, arginase activity is reciprocally coordinated with that of NO synthase to modulate NO-dependent cytotoxicity. The bioinorganic chemistry of arginase is particularly rich because this enzyme is one of very few that specifically requires a spin-coupled Mn2+-Mn2+ cluster for catalytic activity in vitro and in vivo. The 2.1 angstrom-resolution crystal structure of trimeric rat liver arginase reveals that this unique metal cluster resides at the bottom of an active-site cleft that is 15 angstroms deep. Analysis of the structure indicates that arginine hydrolysis is achieved by a metal-activated solvent molecule which symmetrically bridges the two Mn2+ ions.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1RLA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLA OCA].
+
-
 
+
-
==Reference==
+
-
Structure of a unique binuclear manganese cluster in arginase., Kanyo ZF, Scolnick LR, Ash DE, Christianson DW, Nature. 1996 Oct 10;383(6600):554-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8849731 8849731]
+
-
[[Category: Arginase]]
+
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
-
[[Category: Single protein]]
+
[[Category: Ash D]]
-
[[Category: Ash, D.]]
+
[[Category: Christianson DW]]
-
[[Category: Christianson, D.]]
+
[[Category: Kanyo Z]]
-
[[Category: Kanyo, Z.]]
+
[[Category: Scolnick L]]
-
[[Category: Scolnick, L.]]
+
-
[[Category: MN]]
+
-
[[Category: arginine metabolism]]
+
-
[[Category: hydrolase]]
+
-
[[Category: magnesium]]
+
-
[[Category: urea cycle]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:08 2008''
+

Current revision

THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE

PDB ID 1rla

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools